Literature summary for 3.1.1.101 extracted from

Wei, R.; Oeser, T.; Schmidt, J.; Meier, R.; Barth, M.; Then, J.; Zimmermann, W.
Engineered bacterial polyester hydrolases efficiently degrade polyethylene terephthalate due to relieved product inhibition (2016), Biotechnol. Bioeng., 113, 1658-1665 .

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Protein Variants

Protein Variants	Comment	Organism
G62A	mutant enzyme shows highly increased activity in hydrolyzing PET films and fibers. The mutant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme. Kinetic analysis based on the released PET hydrolysis products confirms the superior hydrolytic activity of G62A with a fourfold higher hydrolysis rate constant and a 1.5fold lower substrate binding constant than those of the wild type enzyme. Mutant enzyme G62A reveals a 5.5fold lower binding constant to the inhibitor than the wild type enzyme indicating that its increased PET hydrolysis activity is the result of a relieved product inhibition by mono-(2-hydroxyethyl) terephthalate	Thermobifida fusca
G62A/I213S	mutant enzyme shows highly increased activity in hydrolyzing PET films and fibers. The mutant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme	Thermobifida fusca

Inhibitors

Inhibitors	Comment	Organism	Structure
mono-(2-hydroxyethyl) terephthalate	strong inhibitor	Thermobifida fusca

Organism

Organism	UniProt	Comment	Textmining
Thermobifida fusca	E5BBQ3	-	-
Thermobifida fusca KW3	E5BBQ3	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(ethylene terephthalate)n + H2O	-	Thermobifida fusca	(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate	-	?
(ethylene terephthalate)n + H2O	-	Thermobifida fusca KW3	(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate	-	?

Synonyms

Synonyms	Comment	Organism
TfCut2	-	Thermobifida fusca

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Release 2023.1 (January 2023)